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Conserved domains on  [gi|887218384|ref|NP_001297470|]
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transforming acidic coiled-coil-containing protein 3 isoform 1 [Mus musculus]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 435-631 8.47e-84

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 261.53  E-value: 8.47e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  435 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 507
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  508 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 587
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 887218384  588 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 631
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
rne super family cl35953
ribonuclease E; Reviewed
 144-294 6.32e-04

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  144 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 213
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  214 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 291
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 887218384  292 IEP 294
Cdd:PRK10811 1001 VAP 1003
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 435-631 8.47e-84

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 261.53  E-value: 8.47e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  435 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 507
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  508 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 587
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 887218384  588 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 631
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 417-622 3.22e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 417 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKiaykSLEEAEKQRELKEIA 496
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 497 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 558
Cdd:COG3883   81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887218384 559 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 622
Cdd:COG3883  155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 433-625 2.80e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   433 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 500
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   501 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 580
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 887218384   581 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 625
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
PTZ00121 PTZ00121
MAEBL; Provisional
 453-625 2.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  453 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 529
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  530 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 609
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                         170
                  ....*....|....*.
gi 887218384  610 EMTLEQKTKEIDELTR 625
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
rne PRK10811
ribonuclease E; Reviewed
 144-294 6.32e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  144 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 213
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  214 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 291
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 887218384  292 IEP 294
Cdd:PRK10811 1001 VAP 1003
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 435-631 8.47e-84

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 261.53  E-value: 8.47e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  435 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 507
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  508 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 587
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 887218384  588 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 631
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 417-622 3.22e-07

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 417 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKiaykSLEEAEKQRELKEIA 496
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 497 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 558
Cdd:COG3883   81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887218384 559 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 622
Cdd:COG3883  155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 432-625 2.00e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 432 VLKY------SQKDLDAVvnvmqQENL--------ELKSKYEDLNT------KYLEMGKSVDEFEKIAY-KSLEEAEKQR 490
Cdd:COG1196  167 ISKYkerkeeAERKLEAT-----EENLerledilgELERQLEPLERqaekaeRYRELKEELKELEAELLlLKLRELEAEL 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 491 ELkeiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKiHA 570
Cdd:COG1196  242 EE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ER 317

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 887218384 571 EEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTR 625
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
459-637 2.26e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 459 EDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDL---FKRFEKRKEVI 535
Cdd:COG4717   49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 536 EGYQKNEEsLKKYVGECIVKIEKEGQRYQALKiHAEEKLRLANEEIAQVHSKAQAEV----LALQASLRKAQMQNHSLEM 611
Cdd:COG4717  129 PLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQ 206

                        170       180
                 ....*....|....*....|....*.
gi 887218384 612 TLEQKTKEIDELTRICDDLISKMEKI 637
Cdd:COG4717  207 RLAELEEELEEAQEELEELEEELEQL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 433-625 2.80e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   433 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 500
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   501 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 580
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 887218384   581 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 625
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
PTZ00121 PTZ00121
MAEBL; Provisional
 453-625 2.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  453 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 529
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  530 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 609
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                         170
                  ....*....|....*.
gi 887218384  610 EMTLEQKTKEIDELTR 625
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
PTZ00121 PTZ00121
MAEBL; Provisional
 453-636 3.04e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  453 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 532
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  533 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKlRLANEEIAQVHSKAQAEVLALQA-SLRKAQ-MQNHSLE 610
Cdd:PTZ00121 1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAeEAKKAEeAKKKAEE 1468

                         170       180
                  ....*....|....*....|....*.
gi 887218384  611 MTLEQKTKEIDELTRICDDLISKMEK 636
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEE 1494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 436-616 5.18e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   436 SQKDLDA-VVNVMQQENLELKSKYEDLNtkylemgKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADL 514
Cdd:TIGR02168  330 SKLDELAeELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   515 NSMEKSFSDLFKRFEKRKEVIEGYQKN-EESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVL 593
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALD 478

                          170       180
                   ....*....|....*....|...
gi 887218384   594 ALQASLRKAQMQNHSLEMTLEQK 616
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 439-623 6.75e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   439 DLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAED-------KIQKVLKERDQLN 511
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneEAANLRERLESLE 830

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   512 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLkkyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQA- 590
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELEELSEELREl 906

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 887218384   591 --EVLALQASLRKAQMQNHSLEMTLEQKTKEIDEL 623
Cdd:TIGR02168  907 esKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 448-625 1.26e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 448 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKR 527
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 528 FEKRKEVIEG-----YQKNEESLKKYV--GECIVKIEKEGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQA 597
Cdd:COG4942   99 LEAQKEELAEllralYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|....*...
gi 887218384 598 SLRKAQMQNHSLEMTLEQKTKEIDELTR 625
Cdd:COG4942  179 LLAELEEERAALEALKAERQKLLARLEK 206
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
453-603 2.24e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 453 ELKSKYEDLN------TKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEiaedKIQKVLKERDQLNADLNSMEKSFSDLFK 526
Cdd:PRK03918 277 ELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEK 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 527 RFEKRKEVIEGYQK------NEESLKKYV-GECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQAsL 599
Cdd:PRK03918 353 RLEELEERHELYEEakakkeELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-L 431


                 ....
gi 887218384 600 RKAQ 603
Cdd:PRK03918 432 KKAK 435
PTZ00121 PTZ00121
MAEBL; Provisional
 453-636 2.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  453 ELKSKYEDLntKYLEMGKSVDEFEKIAykslEEAEKQRELKEIAE------DKIQKVLKERDQLNADLNSMEKSFSDLFK 526
Cdd:PTZ00121 1287 EEKKKADEA--KKAEEKKKADEAKKKA----EEAKKADEAKKKAEeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  527 RFEKRKEVIEgyQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQA-SLRKA-QM 604
Cdd:PTZ00121 1361 AAEEKAEAAE--KKKEEAKKK--ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeEKKKAdEA 1436

                         170       180       190
                  ....*....|....*....|....*....|..
gi 887218384  605 QNHSLEMTLEQKTKEIDELTRICDDLISKMEK 636
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 448-635 2.65e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.18  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 448 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSL-EEAEKQRELKEIAEDKIQKVLKERDQL--NADLNSMEKSFSDL 524
Cdd:COG5185  235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgENAESSKRLNENANNLIKQFENTKEKIaeYTKSIDIKKATESL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 525 ---FKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALK-----IHAEEKLRLANEEI----AQVHSKAQAEV 592
Cdd:COG5185  315 eeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienIVGEVELSKSSEELdsfkDTIESTKESLD 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 887218384 593 LALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKME 635
Cdd:COG5185  395 EIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 472-623 3.15e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   472 VDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKsFSDLFKRFEKRK--EVIEGYQKNEESLKKYV 549
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 887218384   550 GEcIVKIEKEGQ----RYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDEL 623
Cdd:TIGR02169  244 RQ-LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
rne PRK10811
ribonuclease E; Reviewed
 144-294 6.32e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  144 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 213
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  214 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 291
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 887218384  292 IEP 294
Cdd:PRK10811 1001 VAP 1003
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 482-637 9.24e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   482 SLEEAEKQRelkEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQ 561
Cdd:TIGR02168  692 KIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   562 RY---QALKIHAEEKLRLANEEIAQV----------HSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICD 628
Cdd:TIGR02168  769 RLeeaEEELAEAEAEIEELEAQIEQLkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848


                   ....*....
gi 887218384   629 DLISKMEKI 637
Cdd:TIGR02168  849 ELSEDIESL 857
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 429-630 1.02e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.35  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   429 IVDVLKYSQKDLDAVVNVMQQENLEL---KSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLK 505
Cdd:TIGR01612  756 ILEDFKNKEKELSNKINDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIIN 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   506 ERDQLNAD------------------LNSMEKSFSDLFKRF--EKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQA 565
Cdd:TIGR01612  836 EMKFMKDDflnkvdkfinfennckekIDSEHEQFAELTNKIkaEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINT 915

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 887218384   566 LKiHAEEKLRL---ANEEIAQVHSKAQAEVLALQASLRKAQMQNhSLEMTLEQK-----TKEIDELTRICDDL 630
Cdd:TIGR01612  916 LK-KVDEYIKIcenTKESIEKFHNKQNILKEILNKNIDTIKESN-LIEKSYKDKfdntlIDKINELDKAFKDA 986
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 449-637 1.57e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   449 QENLElksKYEDLNTkylEMGKSVDEFEKIAYKSLEEAEKQRELKEI------------------AEDKIQKVLKERDQL 510
Cdd:TIGR02168  185 RENLD---RLEDILN---ELERQLKSLERQAEKAERYKELKAELRELelallvlrleelreeleeLQEELKEAEEELEEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   511 NADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKkyvgECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK--- 587
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKlde 334

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 887218384   588 --------------AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 637
Cdd:TIGR02168  335 laeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
PTZ00121 PTZ00121
MAEBL; Provisional
 453-637 1.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  453 ELKSKYEDLNTKYLEMGKSVDEF----EKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSME--KSFSDLFK 526
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKK 1709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  527 RFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLAneeiaqvHSKAQAEVLALQASLRKAQMQN 606
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA-------HLKKEEEKKAEEIRKEKEAVIE 1782

                         170       180       190
                  ....*....|....*....|....*....|.
gi 887218384  607 HSLEMTLEQKTKEIDELTRicdDLISKMEKI 637
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIK---DIFDNFANI 1810
PRK01156 PRK01156
chromosome segregation protein; Provisional
 431-630 1.78e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 431 DVLKYSQKDLDAVVNVMQQENLELKSKYEDLNtkylEMGKSVDEFEKIayKSLEEAEKQRelkeiAEDKIQKVLKERDQL 510
Cdd:PRK01156 169 DKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKS--HSITLKEIER-----LSIEYNNAMDDYNNL 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 511 NADLNSMeKSFSDLFKRFEKRKEVIEG-----------YQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKlrlane 579
Cdd:PRK01156 238 KSALNEL-SSLEDMKNRYESEIKTAESdlsmeleknnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK------ 310

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 887218384 580 eiAQVHSKAQAEVLALQASLRKAQMQnHSLEMTLEQKTKEIDELTRICDDL 630
Cdd:PRK01156 311 --KQILSNIDAEINKYHAIIKKLSVL-QKDYNDYIKKKSRYDDLNNQILEL 358
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
 422-600 2.02e-03

Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.


Pssm-ID: 464151 [Multi-domain]  Cd Length: 295  Bit Score: 40.70  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  422 GLLPAEPIVdvLKYSQKDLDAVVNVMQQEnlelkskyedlntkylemgksvdefekiaykslEEAEKQRELKEIAEDKIQ 501
Cdd:pfam14362  92 GVVISEPLE--LKIFEKEIDRELLEIQQE---------------------------------EADAAKAQLAAAYRARLA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  502 KVLKERDQLNADLNSMEKSFSDLFKrfEKRKEvIEGYQKNEESLKKYVGECIVK---IEKEGQRYQALKIHAEEKLRLAN 578
Cdd:pfam14362 137 ELEAQIAALDAEIDAAEARLDALQA--EARCE-LDGTPGTGTGVPGDGPVAKTKqaqLDAAQAELAALQAQNDARLAALR 213

                         170       180
                  ....*....|....*....|..
gi 887218384  579 EEIAQVHSKAQAEVLALQASLR 600
Cdd:pfam14362 214 AELARLTAERAAARARSQAAID 235
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 448-636 2.72e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.61  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  448 QQENLELKSKYEDLNTKYLE----MGKSVDEFEKIayksLEEAEKQR----ELKE----IAEDKIQKVLKER-DQLNADL 514
Cdd:pfam06160 120 REEVEELKDKYRELRKTLLAnrfsYGPAIDELEKQ----LAEIEEEFsqfeELTEsgdyLEAREVLEKLEEEtDALEELM 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  515 NSMEKSFSDLFKRFEKR-KEVIEGYQKNEEslKKY------VGECIVKIEKEGQRYQA----LKI-HAEEKLRLANEEIA 582
Cdd:pfam06160 196 EDIPPLYEELKTELPDQlEELKEGYREMEE--EGYalehlnVDKEIQQLEEQLEENLAllenLELdEAEEALEEIEERID 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  583 QVHSKAQAEVLA----------LQASLRKAQMQNHSL--EMTLEQKT---------------KEIDELTRICDDLISKME 635
Cdd:pfam06160 274 QLYDLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELkeELERVQQSytlnenelervrgleKQLEELEKRYDEIVERLE 353


                  .
gi 887218384  636 K 636
Cdd:pfam06160 354 E 354
PRK12704 PRK12704
phosphodiesterase; Provisional
 470-583 2.77e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 470 KSVDEFEKIAYKSLEEAEKqrELKEIAEDKI----QKVLKERDQLNADLNSMEKSFSDLFKR--------------FEKR 531
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKK--EAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRllqkeenldrklelLEKR 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 887218384 532 KEVIEGYQKNEESLKKYVGECIVKIEkegqryqalKIHAEEKLRLanEEIAQ 583
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELE---------ELIEEQLQEL--ERISG 149
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
453-637 3.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 453 ELKSKYEDLNtKYLEMGKSVDEFEKIAYKSLEeaEKQRELKEIaEDKIQKVLKERDQLNADLnsmeksfsdlfKRFEKRK 532
Cdd:PRK03918 173 EIKRRIERLE-KFIKRTENIEELIKEKEKELE--EVLREINEI-SSELPELREELEKLEKEV-----------KELEELK 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 533 EVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEkLRLANEEIAQVHSKAQaEVLALQASLRKAQMQNHSLEMT 612
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKR 315

                        170       180
                 ....*....|....*....|....*
gi 887218384 613 LEQKTKEIDELTRICDDLISKMEKI 637
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERL 340
rne PRK10811
ribonuclease E; Reviewed
 99-276 3.20e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384   99 PLAPVDDAPVV-QMAAEILRAEGELQEgiltssslSASTSLLDSELVTPPIEPVLEPSHqglEPVLESELVTPPVEPVlE 177
Cdd:PRK10811  846 PVVRPQDVQVEeQREAEEVQVQPVVAE--------VPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVV-E 913

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  178 PSHQEL--EPVLES-ELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHqglEPVLESELVTPPIEPVLEPSHQG 254
Cdd:PRK10811  914 TTHPEViaAPVTEQpQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAAE 990

                         170       180
                  ....*....|....*....|....*
gi 887218384  255 L--EPVLDSELVTPPI-EPVLEPSH 276
Cdd:PRK10811  991 VetVTAVEPEVAPAQVpEATVEHNH 1015
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 437-637 3.73e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  437 QKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEK------IAYKSL---------EEAEKQRELKEIAEDKIQ 501
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsRSINKIkqnleqkqkELKSKEKELKKLNEEKKE 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384  502 -----KVLKER--------DQLNADLNSMEKSFSDLFKRFEKRKEViegyqKNEESLKKYVGECIVKIEKegqryqaLKi 568
Cdd:TIGR04523 508 leekvKDLTKKisslkekiEKLESEKKEKESKISDLEDELNKDDFE-----LKKENLEKEIDEKNKEIEE-------LK- 574

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887218384  569 HAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 637
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
453-637 4.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 453 ELKSKYEDLNTKYLEmgKSVDEFEKIAYKSLEEAEKQRELKEIAEdKIQKVLKERDQLNADLNSMEKSFSDLFKR----- 527
Cdd:PRK03918 507 ELEEKLKKYNLEELE--KKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKEleelg 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 528 FEKRKEVIEGYQKNEESLKKYVGecIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNH 607
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 887218384 608 --------SLEMTLEQKTKEIDELTRICDDLISKMEKI 637
Cdd:PRK03918 662 eelreeylELSRELAGLRAELEELEKRREEIKKTLEKL 699
PRK12704 PRK12704
phosphodiesterase; Provisional
 529-637 5.11e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 529 EKRKEVIEGYQKNEESLKKyvgECIVKIEKEgqrYQALKIHAEEKLRLANEEIAQVHSKAQAEVLAL---QASLRKAQMQ 605
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKK---EALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 887218384 606 NHSLEMTLEQKTKEIDELTRICDDLISKMEKI 637
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 477-592 5.78e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.28  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 477 KIAYKSLEEAEKQRELKEIAEDKIQKvlkERDQLNADLNSMEKSFSDLFKRFEKRKEVIegyqkNEESLKKYVGEcIVKI 556
Cdd:COG2825   25 KIGVVDVQRILQESPEGKAAQKKLEK---EFKKRQAELQKLEKELQALQEKLQKEAATL-----SEEERQKKERE-LQKK 95

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 887218384 557 EKEGQRYQALkihAEEKLRLA-NEEIAQVHSKAQAEV 592
Cdd:COG2825   96 QQELQRKQQE---AQQDLQKRqQELLQPILEKIQKAI 129
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 481-602 8.64e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 8.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887218384 481 KSLEEAEKQRELKE--IAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEK 558
Cdd:PRK09510  72 KSAKRAEEQRKKKEqqQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 887218384 559 EGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKA 602
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKA 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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